1ugh
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ugh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_pbs2 Bacillus phage pbs2] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UGH FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ugh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_pbs2 Bacillus phage pbs2] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UGH FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] </span></td></tr> | + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ugh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ugh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ugh RCSB], [http://www.ebi.ac.uk/pdbsum/1ugh PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ugh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ugh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ugh RCSB], [http://www.ebi.ac.uk/pdbsum/1ugh PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
== Disease == | == Disease == | ||
[[http://www.uniprot.org/uniprot/UNG_HUMAN UNG_HUMAN]] Defects in UNG are a cause of immunodeficiency with hyper-IgM type 5 (HIGM5) [MIM:[http://omim.org/entry/608106 608106]]. A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections.<ref>PMID:12958596</ref> <ref>PMID:15967827</ref> | [[http://www.uniprot.org/uniprot/UNG_HUMAN UNG_HUMAN]] Defects in UNG are a cause of immunodeficiency with hyper-IgM type 5 (HIGM5) [MIM:[http://omim.org/entry/608106 608106]]. A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections.<ref>PMID:12958596</ref> <ref>PMID:15967827</ref> | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Uridine nucleosidase]] | [[Category: Uridine nucleosidase]] | ||
| - | [[Category: Arvai, A S | + | [[Category: Arvai, A S]] |
| - | [[Category: Kavli, B | + | [[Category: Kavli, B]] |
| - | [[Category: Krokan, H E | + | [[Category: Krokan, H E]] |
| - | [[Category: Mol, C D | + | [[Category: Mol, C D]] |
| - | [[Category: Mosbaugh, D W | + | [[Category: Mosbaugh, D W]] |
| - | [[Category: Sanderson, R J | + | [[Category: Sanderson, R J]] |
| - | [[Category: Slupphaug, G | + | [[Category: Slupphaug, G]] |
| - | [[Category: Tainer, J A | + | [[Category: Tainer, J A]] |
[[Category: Enzyme-inhibitor complex]] | [[Category: Enzyme-inhibitor complex]] | ||
[[Category: Glycosylase]] | [[Category: Glycosylase]] | ||
Revision as of 13:02, 6 January 2015
CRYSTAL STRUCTURE OF HUMAN URACIL-DNA GLYCOSYLASE IN COMPLEX WITH A PROTEIN INHIBITOR: PROTEIN MIMICRY OF DNA
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